Histone H2A type 1

Functionⁱ

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functionⁱ

DNA binding Source: UniProtKB-KW
protein heterodimerization activity Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding

Molecular function

DNA-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Histone H2A type 1
Organismⁱ	Xenopus laevis (African clawed frog)
Taxonomic identifierⁱ	8355 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Organism-specific databases

Xenbaseⁱ	XB-GENE-6493983 h2afx

Xenbaseⁱ

XB-GENE-6493983 h2afx

Keywords - Cellular componentⁱ

Chromosome, Nucleosome core, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed
ChainⁱPRO_0000055294	2 – 130	Histone H2A type 1Add BLAST		129

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineBy similarity	1
Modified residueⁱ	2	PhosphoserineBy similarity	1
Modified residueⁱ	6	N6-(2-hydroxyisobutyryl)lysineBy similarity	1
Modified residueⁱ	6	N6-acetyllysineBy similarity	1
Modified residueⁱ	10	N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity	1
Modified residueⁱ	10	N6-succinyllysineBy similarity	1
Cross-linkⁱ	14	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	16	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	37	N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity	1
Modified residueⁱ	75	N6-(2-hydroxyisobutyryl)lysineBy similarity	1
Modified residueⁱ	76	N6-(2-hydroxyisobutyryl)lysineBy similarity	1
Modified residueⁱ	96	N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity	1
Modified residueⁱ	96	N6-succinyllysineBy similarity	1
Modified residueⁱ	105	N5-methylglutamineBy similarity	1
Modified residueⁱ	119	N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity	1
Cross-linkⁱ	120	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationⁱ

Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events (By similarity).By similarity

Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription (By similarity).By similarity

Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (By similarity).By similarity

Keywords - PTMⁱ

Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEⁱ	P06897

PRIDEⁱ

P06897

Interactionⁱ

Subunit structureⁱ

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

GO - Molecular functionⁱ

protein heterodimerization activity Source: InterPro

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	592527, 2 interactors
Database of interacting proteins More...DIPⁱ	DIP-39144N
IntActⁱ	P06897, 10 interactors

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	6 – 8	Combined sources	3
Beta strandⁱ	9 – 13	Combined sources	5
Helixⁱ	18 – 22	Combined sources	5
Helixⁱ	28 – 37	Combined sources	10
Beta strandⁱ	42 – 44	Combined sources	3
Helixⁱ	47 – 73	Combined sources	27
Beta strandⁱ	77 – 79	Combined sources	3
Helixⁱ	81 – 89	Combined sources	9
Helixⁱ	92 – 97	Combined sources	6
Turnⁱ	98 – 100	Combined sources	3
Beta strandⁱ	101 – 103	Combined sources	3
Helixⁱ	114 – 116	Combined sources	3
Beta strandⁱ	117 – 119	Combined sources	3
Helixⁱ	120 – 122	Combined sources	3
Turnⁱ	124 – 126	Combined sources	3

3D structure databases

ProteinModelPortalⁱ	P06897
SMRⁱ	P06897
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P06897

EvolutionaryTraceⁱ

P06897

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the histone H2A family.Curated

Phylogenomic databases

HOVERGENⁱ	HBG009342
KEGG Orthology (KO) More...KOⁱ	K11251

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00074 H2A, 1 hit
Gene3Dⁱ	1.10.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR009072 Histone-fold IPR002119 Histone_H2A IPR007125 Histone_H2A/H2B/H3 IPR032454 Histone_H2A_C IPR032458 Histone_H2A_CS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00125 Histone, 1 hit PF16211 Histone_H2A_C, 1 hit
PRINTSⁱ	PR00620 HISTONEH2A
SMARTⁱ	View protein in SMART SM00414 H2A, 1 hit
SUPFAMⁱ	SSF47113 SSF47113, 1 hit
PROSITEⁱ	View protein in PROSITE PS00046 HISTONE_H2A, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P06897-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV 
        60         70         80         90        100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG 
       110        120        130
VTIAQGGVLP NIQSVLLPKK TESAKSAKSK

Length:130

Mass (Da):13,966

Last modified:January 23, 2007 - v2

Checksum:ⁱ09946ABF27FA52A9

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X03018 Genomic DNA Translation: CAA26817.1 M21287 Genomic DNA Translation: AAA49769.1 BC106331 mRNA Translation: AAI06332.1
PIRⁱ	H24510 HSXLA1
NCBI Reference Sequences More...RefSeqⁱ	NP_001089684.1, NM_001096215.1
UniGeneⁱ	Xl.19141

Genome annotation databases

GeneIDⁱ	734746
KEGGⁱ	xla:734746

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
P06897	Histone H2A type 4		RAT		130
UPI00071E208E		CALPG		161
Histone H2A		SAIBB		130
Histone H2A		CALJA		130
histone H2A type 3		ODORO		130
+217

Protein	Similar proteins		Species	Score	Length
P06897	Histone H2A type 1-C	)	HUMAN		130
Histone H2A type 1-C		RAT		130
Histone H2A		MACMU		130
Histone H2A		PANTR		130
histone H2A type 1-C-like		LEPWE		130
+1662

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X03018 Genomic DNA Translation: CAA26817.1 M21287 Genomic DNA Translation: AAA49769.1 BC106331 mRNA Translation: AAI06332.1
PIRⁱ	H24510 HSXLA1
NCBI Reference Sequences More...RefSeqⁱ	NP_001089684.1, NM_001096215.1
UniGeneⁱ	Xl.19141

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1AOI	X-ray	2.80	C/G	5-120	[»]
	1KX3	X-ray	2.00	C/G	2-130	[»]
	1KX4	X-ray	2.60	C/G	2-130	[»]
	1KX5	X-ray	1.94	C/G	2-130	[»]
	1M18	X-ray	2.45	C/G	2-130	[»]
	1M19	X-ray	2.30	C/G	2-130	[»]
	1M1A	X-ray	2.65	C/G	2-130	[»]
	1P34	X-ray	2.70	C/G	2-130	[»]
	1P3A	X-ray	3.00	C/G	2-130	[»]
	1P3B	X-ray	3.00	C/G	2-130	[»]
	1P3F	X-ray	2.90	C/G	2-130	[»]
	1P3G	X-ray	2.70	C/G	2-130	[»]
	1P3I	X-ray	2.30	C/G	2-130	[»]
	1P3K	X-ray	2.90	C/G	2-130	[»]
	1P3L	X-ray	2.40	C/G	2-130	[»]
	1P3M	X-ray	2.90	C/G	2-130	[»]
	1P3O	X-ray	2.75	C/G	2-130	[»]
	1P3P	X-ray	2.70	C/G	2-130	[»]
	1S32	X-ray	2.05	C/G	2-120	[»]
	1ZBB	X-ray	9.00	C/G/c/g	2-130	[»]
	1ZLA	X-ray	2.90	C/G	2-130	[»]
	2FJ7	X-ray	3.20	C/G	2-130	[»]
	2NZD	X-ray	2.65	C/G	2-120	[»]
	3B6F	X-ray	3.45	C/G	2-130	[»]
	3B6G	X-ray	3.45	C/G	2-130	[»]
	3C1B	X-ray	2.20	C/G	2-130	[»]
	3C1C	X-ray	3.15	C/G	2-130	[»]
	3KUY	X-ray	2.90	C/G	2-120	[»]
	3KWQ	X-ray	3.50	C/G	15-121	[»]
	3LJA	X-ray	2.75	C/G	2-130	[»]
	3MNN	X-ray	2.50	C/G	2-120	[»]
	3O62	X-ray	3.22	C/G	2-130	[»]
	3REH	X-ray	2.50	C/G	2-130	[»]
	3REI	X-ray	2.65	C/G	2-130	[»]
	3REJ	X-ray	2.55	C/G	2-130	[»]
	3REK	X-ray	2.60	C/G	2-130	[»]
	3REL	X-ray	2.70	C/G	2-130	[»]
	3TU4	X-ray	3.00	C/G	2-130	[»]
	3UT9	X-ray	2.20	C/G	2-130	[»]
	3UTA	X-ray	2.07	C/G	2-130	[»]
	3UTB	X-ray	2.20	C/G	2-130	[»]
	4J8U	X-ray	2.38	C/G	2-130	[»]
	4J8V	X-ray	2.58	C/G	2-130	[»]
	4J8W	X-ray	2.41	C/G	2-130	[»]
	4J8X	X-ray	2.87	C/G	2-130	[»]
	4LD9	X-ray	3.31	C/G	1-130	[»]
	4R8P	X-ray	3.28	C/G	2-130	[»]
	4WU8	X-ray	2.45	C/G	2-130	[»]
	4WU9	X-ray	2.60	C/G	2-130	[»]
	4XUJ	X-ray	3.18	C/G	2-130	[»]
	4XZQ	X-ray	2.40	C/G	15-121	[»]
	4YS3	X-ray	3.00	C/G	15-121	[»]
	4Z66	X-ray	2.50	C/G	15-121	[»]
	4ZUX	X-ray	3.82	C/G/M/Q	1-130	[»]
	5CP6	X-ray	2.60	C/G	2-130	[»]
	5DNM	X-ray	2.81	C/G	2-130	[»]
	5DNN	X-ray	2.80	C/G	2-130	[»]
	5E5A	X-ray	2.81	C/G	1-130	[»]
	5F99	X-ray	2.63	C/G	2-130	[»]
	5G2E	X-ray	6.70	C/G/K/O/S/W	14-119	[»]
	5HQ2	X-ray	4.50	G	2-130	[»]
	5MLU	X-ray	2.80	C/G	15-119	[»]
	5NL0	X-ray	5.40	C/G/M	2-130	[»]
5O9G	electron microscopy	4.80	C/G	1-130	[»]
5OMX	X-ray	2.32	C/G	2-130	[»]
5ONG	X-ray	2.80	C/G	2-130	[»]
5ONW	X-ray	2.80	C/G	2-130	[»]
5OXV	X-ray	6.72	C/G/M/Q	1-130	[»]
5OY7	X-ray	5.77	C/G/K/O/S/W/a/e	1-130	[»]
5X0X	electron microscopy	3.97	C/G	1-130	[»]
5X0Y	electron microscopy	4.69	C/G	2-130	[»]
5XF6	X-ray	2.63	C/G	2-130	[»]
ProteinModelPortalⁱ	P06897
SMRⁱ	P06897
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	592527, 2 interactors
Database of interacting proteins More...DIPⁱ	DIP-39144N
IntActⁱ	P06897, 10 interactors

Proteomic databases

PRIDEⁱ	P06897

PRIDEⁱ

P06897

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	734746
KEGGⁱ	xla:734746

Organism-specific databases

CTDⁱ	734746
Xenbaseⁱ	XB-GENE-6493983 h2afx

Phylogenomic databases

HOVERGENⁱ	HBG009342
KEGG Orthology (KO) More...KOⁱ	K11251

Miscellaneous databases

EvolutionaryTraceⁱ	P06897

EvolutionaryTraceⁱ

P06897

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00074 H2A, 1 hit
Gene3Dⁱ	1.10.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR009072 Histone-fold IPR002119 Histone_H2A IPR007125 Histone_H2A/H2B/H3 IPR032454 Histone_H2A_C IPR032458 Histone_H2A_CS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00125 Histone, 1 hit PF16211 Histone_H2A_C, 1 hit
PRINTSⁱ	PR00620 HISTONEH2A
SMARTⁱ	View protein in SMART SM00414 H2A, 1 hit
SUPFAMⁱ	SSF47113 SSF47113, 1 hit
PROSITEⁱ	View protein in PROSITE PS00046 HISTONE_H2A, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	H2A1_XENLA
Accessionⁱ	P06897Primary (citable) accession number: P06897 Secondary accession number(s): Q3B8I8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
	Last sequence update:	January 23, 2007
	Last modified:	March 28, 2018
	This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

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Annotation systems

Supporting data

UniProtKB - P06897 (H2A1_XENLA)

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Nucleus

Other locations

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ